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A0A0F8D2F2 · A0A0F8D2F2_9EURY

  • Protein
    Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain likely plays a direct catalytic role in this reaction. The Bud32 domain probably displays kinase activity that regulates Kae1 function.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Note: Binds 1 Fe2+ ion per subunit.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site113Fe cation (UniProtKB | ChEBI)
Binding site117Fe cation (UniProtKB | ChEBI)
Binding site134Fe cation (UniProtKB | ChEBI)
Binding site134-138L-threonylcarbamoyladenylate (UniProtKB | ChEBI)
Binding site166L-threonylcarbamoyladenylate (UniProtKB | ChEBI)
Binding site179L-threonylcarbamoyladenylate (UniProtKB | ChEBI)
Binding site183L-threonylcarbamoyladenylate (UniProtKB | ChEBI)
Binding site262L-threonylcarbamoyladenylate (UniProtKB | ChEBI)
Binding site290Fe cation (UniProtKB | ChEBI)
Binding site355-363ATP (UniProtKB | ChEBI)
Binding site377ATP (UniProtKB | ChEBI)
Active site464Proton acceptor; for kinase activity

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular ComponentEKC/KEOPS complex
Molecular FunctionATP binding
Molecular Functionhistone H2AS1 kinase activity
Molecular Functioniron ion binding
Molecular Functionmetalloendopeptidase activity
Molecular FunctionN(6)-L-threonylcarbamoyladenine synthase activity
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine/tyrosine kinase activity
Molecular Functionzinc ion binding
Biological Processprotein phosphorylation
Biological ProcesstRNA threonylcarbamoyladenosine modification

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein

Including 2 domains:

  • Recommended name
    tRNA N6-adenosine threonylcarbamoyltransferase
  • EC number
  • Alternative names
    • tRNA threonylcarbamoyladenosine biosynthesis protein Kae1
    • t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1
  • Recommended name
    Serine/threonine-protein kinase Bud32
  • EC number

Gene names

    • ORF names
      EO98_06650

Organism names

  • Taxonomic identifier
  • Strain
    • 2.H.T.1A.6
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Methanomicrobia > Methanosarcinales > Methanosarcinaceae > Methanosarcina

Accessions

  • Primary accession
    A0A0F8D2F2

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Component of the KEOPS complex that consists of Kae1, Bud32, Cgi121 and Pcc1; the whole complex dimerizes.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-329Kae1
Domain349-547Protein kinase

Sequence similarities

In the C-terminal section; belongs to the protein kinase superfamily. Tyr protein kinase family. BUD32 subfamily.
In the N-terminal section; belongs to the KAE1 / TsaD family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    547
  • Mass (Da)
    60,565
  • Last updated
    2015-07-22 v1
  • MD5 Checksum
    585013E0C00F32A776A6DDB566DAE707
MKNTFILGIEGTAWNLSAAIVTETEIIAEVTETYKPEKGGIHPREAAQHHAKYAASVIKKLLAEAKEKGVEPSDIDGIAFSQGPGLGPCLRTVATAARVLSLSLGIPLIGVNHCIAHIEIGIWKTPAKDPVVLYVSGANSQVISYMEGRYRVFGETLDIGLGNALDKFARGAGLSHPGGPKIETCAKDAKQYIHLPYVIKGMDLSFSGLSTASSEALKKATLEDVCYSYQETAFAMVVEVAERALAHTGKKEVLLAGGVGANTRLREMLNKMCEARDATFYVPEKRFMGDNGTMIAYTGLLMYKSGNTLSIEDSRVNPSFRTDDVKVTWIKEEDMKRVPEISPETFFRTPPGEMLDSGAEAVVYLEDGPEGKKVLVKERVPKVYRHREIDERIRRERNRAEARLMSEARRTGVPTPIIYDVEEFKLKMQFIEGVPIKYLITPEVSEKVGELVGKLHSSGIVHGDLTTSNLLLAGERLYLIDFGLAYFDKSLEARGVDVHVLFQTFESTHRDHETLVKAFEKGYGSTFIDSEDVLRRVEEIKKRARYA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JJOY01000031
EMBL· GenBank· DDBJ
KKG21746.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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